1soh
From Proteopedia
(New page: 200px<br /> <applet load="1soh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1soh" /> '''The structure of human apolipoprotein C-II ...) |
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'''The structure of human apolipoprotein C-II in dodecyl phosphocholine'''<br /> | '''The structure of human apolipoprotein C-II in dodecyl phosphocholine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of human apolipoprotein C-II (apoC-II) in the presence of | + | The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy. The resulting structural information is compared to that available for apoC-II in the presence of sodium dodecyl sulfate, revealing a high level of overall similarity but several significant differences. These findings further our understandings of the structural basis for apoC-II function. The interactions of the protein with the detergent micelle are probed using intermolecular nuclear Overhauser effects (NOEs) and paramagnetic agents. These interactions are seen across almost the full length of apoC-II and show the periodicity expected for an amphipathic helix interacting with the amphipathic surface of the DPC micelle. Furthermore, we observe specific contacts between lysine residues of apoC-II and protons near the phosphate group of DPC, consistent with the predictions of the so-called "snorkel hypothesis" of the structural basis for the apolipoprotein/lipid interaction (Segrest, J. P., Jackson, R. L., Morrisett, J. D., and Gotto, A. M., Jr. (1974) A molecular theory of lipid-protein interactions in the plasma lipoproteins, FEBS Lett 38, 247-258.). These findings offer the most detailed structural information available for the interaction between an apolipoprotein and the phospholipids of the lipoprotein surface and provide the first direct structural support for the snorkel hypothesis. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1SOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gooley, P | + | [[Category: Gooley, P R.]] |
| - | [[Category: Howlett, G | + | [[Category: Howlett, G J.]] |
| - | [[Category: MacRaild, C | + | [[Category: MacRaild, C A.]] |
[[Category: lipid transport]] | [[Category: lipid transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:34 2008'' |
Revision as of 13:03, 21 February 2008
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The structure of human apolipoprotein C-II in dodecyl phosphocholine
Contents |
Overview
The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy. The resulting structural information is compared to that available for apoC-II in the presence of sodium dodecyl sulfate, revealing a high level of overall similarity but several significant differences. These findings further our understandings of the structural basis for apoC-II function. The interactions of the protein with the detergent micelle are probed using intermolecular nuclear Overhauser effects (NOEs) and paramagnetic agents. These interactions are seen across almost the full length of apoC-II and show the periodicity expected for an amphipathic helix interacting with the amphipathic surface of the DPC micelle. Furthermore, we observe specific contacts between lysine residues of apoC-II and protons near the phosphate group of DPC, consistent with the predictions of the so-called "snorkel hypothesis" of the structural basis for the apolipoprotein/lipid interaction (Segrest, J. P., Jackson, R. L., Morrisett, J. D., and Gotto, A. M., Jr. (1974) A molecular theory of lipid-protein interactions in the plasma lipoproteins, FEBS Lett 38, 247-258.). These findings offer the most detailed structural information available for the interaction between an apolipoprotein and the phospholipids of the lipoprotein surface and provide the first direct structural support for the snorkel hypothesis.
Disease
Known disease associated with this structure: Hyperlipoproteinemia, type Ib OMIM:[608083]
About this Structure
1SOH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine., MacRaild CA, Howlett GJ, Gooley PR, Biochemistry. 2004 Jun 29;43(25):8084-93. PMID:15209504
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